Category
Basic
Description
Peroxidases are present in many diverse plant species and catalyze chemical oxidations, some that may have significance in biotechnological areas like bioremediation. In several recent papers we characterizes a novel peroxidase from the skin of pumpkin that possessed desirable catalytic activities in relation to a class of environmental contaminants call fluorinated phenolics. In the course of these studies, we were able to do genomic analysis on a related plant species curcubita moscata (butternut squash) and identified a peroxidase with very similar sequence. The current study focusses on the characterization of that novel peroxidase in comparison with the pumpkin skin squash. Variations in catalytic properties will then be rationalized with respect to the minor changes in the amino acid sequences between the two species. This study is important because fluorinated aromatics are a growing class of contaminants in soil and wastewater due to their production as waste products in the pharmaceutical and agrochemical industries.
The novel butternut enzyme will be characterized by comparing its electronic absorption properties with those of PKS and HRP (the prototypical peroxidase used in most industry applications), along with catalytic properties with a series of fluorinated organics. In addition, the PKS enzyme has been shown to bind small perfluorinated carboxylic acid derivatives, which opens the door for studies aimed at degrading this important class of compounds (PFAS) by peroxidase enzymes. Comparison of the binding properties of Butternut squash peroxidase with PKS will also be described.
Characterization of Peroxidase from Butternut Squash Skin: Potential Use in Bioremediation
Basic
Peroxidases are present in many diverse plant species and catalyze chemical oxidations, some that may have significance in biotechnological areas like bioremediation. In several recent papers we characterizes a novel peroxidase from the skin of pumpkin that possessed desirable catalytic activities in relation to a class of environmental contaminants call fluorinated phenolics. In the course of these studies, we were able to do genomic analysis on a related plant species curcubita moscata (butternut squash) and identified a peroxidase with very similar sequence. The current study focusses on the characterization of that novel peroxidase in comparison with the pumpkin skin squash. Variations in catalytic properties will then be rationalized with respect to the minor changes in the amino acid sequences between the two species. This study is important because fluorinated aromatics are a growing class of contaminants in soil and wastewater due to their production as waste products in the pharmaceutical and agrochemical industries.
The novel butternut enzyme will be characterized by comparing its electronic absorption properties with those of PKS and HRP (the prototypical peroxidase used in most industry applications), along with catalytic properties with a series of fluorinated organics. In addition, the PKS enzyme has been shown to bind small perfluorinated carboxylic acid derivatives, which opens the door for studies aimed at degrading this important class of compounds (PFAS) by peroxidase enzymes. Comparison of the binding properties of Butternut squash peroxidase with PKS will also be described.
